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Structure paper

TitleAllostery and Conformational Dynamics in cAMP-binding Acyltransferases.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 16588-16600, Year 2014
Publish dateJan 24, 2014 (structure data deposition date)
AuthorsPodobnik, M. / Siddiqui, N. / Rebolj, K. / Nambi, S. / Merzel, F. / Visweswariah, S.S.
External linksJ. Biol. Chem. / PubMed:24748621
MethodsX-ray diffraction
Resolution1.9 - 2.25 Å
Structure data

PDB-4oll:
cAMP-binding acyltransferase from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4onu:
cAMP-binding acyltransferase from Mycobacterium smegmatis, E234A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-4orf:
cAMP-binding acyltransferase from Mycobacterium smegmatis, mutant R95K
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • mycobacterium smegmatis (bacteria)
KeywordsTRANSFERASE / alpha-beta fold / linker peptide / cyclic nucleotide binding domain / acyl-transferase domain / apo-enzyme

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